A method for evaluating the level of soluble β-amyloid(1-40/1-42) in Alzheimer's disease based on the binding of gelsolin to β-amyloid peptides.

In the present work, a new electrochemical strategy for the sensitive and specific detection of soluble β-amyloid Aβ(1-40/1-42) peptides in a rat model of Alzheimer's disease (AD) is described. In contrast to previous antibody-based methods, β-amyloid(1-40/1-42) was quantified based on its binding to gelsolin, a secretory protein present in the cerebrospinal fluid (CSF) and plasma. The level of soluble β-amyloid peptides in the CSF and various brain regions were found with this method to be lower in rats with AD than in normal rats.